ID BAG4_HUMAN Reviewed; 457 AA. AC O95429; O95818; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 25-JAN-2012, entry version 103. DE RecName: Full=BAG family molecular chaperone regulator 4; DE Short=BAG-4; DE AltName: Full=Bcl-2-associated athanogene 4; DE AltName: Full=Silencer of death domains; GN Name=BAG4; Synonyms=SODD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leukemic T-cell; RX MEDLINE=99091615; PubMed=9873016; DOI=10.1074/jbc.274.2.781; RA Takayama S., Xie Z., Reed J.C.; RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone RT regulators."; RL J. Biol. Chem. 274:781-786(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TNFRSF1A AND RP TNFRSF12. RC TISSUE=Leukemic T-cell; RX MEDLINE=99115917; PubMed=9915703; DOI=10.1126/science.283.5401.543; RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.; RT "Prevention of constitutive TNF receptor 1 signaling by silencer of RT death domains."; RL Science 283:543-546(1999). RN [3] RP ERRATUM. RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.; RL Science 283:1852-1852(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP STRUCTURE BY NMR OF 376-457, INTERACTION WITH HSP70, AND MUTAGENESIS RP OF GLU-414; ASP-424; 438-ARG-LYS-439 AND GLN-446. RX MEDLINE=22172832; PubMed=12058034; DOI=10.1074/jbc.M202792200; RA Briknarova K., Takayama S., Homma S., Baker K., Cabezas E., Hoyt D.W., RA Li Z., Satterthwait A.C., Ely K.R.; RT "BAG4/SODD protein contains a short BAG domain."; RL J. Biol. Chem. 277:31172-31178(2002). CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by CC promoting substrate release (By similarity). Prevents constitutive CC TNFRSF1A signaling. CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds CC to the death domain of TNFRSF1A in the absence of TNF and thereby CC prevents binding of adapter molecules such as TRADD or TRAF2. CC Binds to the death domain of TNFRSF12. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Contains 1 BAG domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF095194; AAD16123.2; -; mRNA. DR EMBL; AF111116; AAD05226.1; -; mRNA. DR EMBL; BC038505; AAH38505.2; -; mRNA. DR IPI; IPI00030695; -. DR RefSeq; NP_004865.1; NM_004874.3. DR UniGene; Hs.194726; -. DR PDB; 1M62; NMR; -; A=376-457. DR PDB; 1M7K; NMR; -; A=358-456. DR PDBsum; 1M62; -. DR PDBsum; 1M7K; -. DR ProteinModelPortal; O95429; -. DR SMR; O95429; 376-456. DR IntAct; O95429; 3. DR STRING; O95429; -. DR PhosphoSite; O95429; -. DR PRIDE; O95429; -. DR Ensembl; ENST00000287322; ENSP00000287322; ENSG00000156735. DR GeneID; 9530; -. DR KEGG; hsa:9530; -. DR UCSC; uc003xky.1; human. DR CTD; 9530; -. DR GeneCards; GC08P038051; -. DR H-InvDB; HIX0020972; -. DR HGNC; HGNC:940; BAG4. DR HPA; CAB013716; -. DR HPA; HPA018951; -. DR MIM; 603884; gene. DR neXtProt; NX_O95429; -. DR PharmGKB; PA25240; -. DR eggNOG; prNOG14642; -. DR GeneTree; ENSGT00530000063256; -. DR HOGENOM; HBG268473; -. DR HOVERGEN; HBG004809; -. DR InParanoid; O95429; -. DR OMA; YGNATNE; -. DR OrthoDB; EOG4PG627; -. DR PhylomeDB; O95429; -. DR Pathway_Interaction_DB; ceramidepathway; Ceramide signaling pathway. DR Pathway_Interaction_DB; hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha. DR Pathway_Interaction_DB; tnfpathway; TNF receptor signaling pathway. DR NextBio; 35728; -. DR ArrayExpress; O95429; -. DR Bgee; O95429; -. DR CleanEx; HS_BAG4; -. DR Genevestigator; O95429; -. DR GermOnline; ENSG00000156735; Homo sapiens. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0051087; F:chaperone binding; IEA:InterPro. DR GO; GO:0005057; F:receptor signaling protein activity; TAS:ProtInc. DR GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB. DR GO; GO:0006457; P:protein folding; TAS:ProtInc. DR InterPro; IPR003103; BAG_domain. DR KO; K09558; -. DR Pfam; PF02179; BAG; 1. DR SMART; SM00264; BAG; 1. DR PROSITE; PS51035; BAG; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Complete proteome; Cytoplasm; KW Reference proteome. FT CHAIN 1 457 BAG family molecular chaperone regulator FT 4. FT /FTId=PRO_0000088870. FT DOMAIN 379 456 BAG. FT MUTAGEN 414 414 E->A: Reduces interaction with HSP70. FT MUTAGEN 424 424 D->A: Abolishes interaction with HSP70. FT MUTAGEN 438 439 RK->AA: Reduces interaction with HSP70. FT MUTAGEN 446 446 Q->A: Abolishes interaction with HSP70. FT HELIX 380 399 FT HELIX 407 423 FT HELIX 432 456 SQ SEQUENCE 457 AA; 49594 MW; B89D59E8118684A3 CRC64; MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW RVRGGGPAET TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS NYWNSTARSR APYPSTYPVR PELQGQSLNS YTNGAYGPTY PPGPGANTAS YSGAYYAPGY TQTSYSTEVP STYRSSGNSP TPVSRWIYPQ QDCQTEAPPL RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE DAWASPGAYG MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN ATSDHPNNQD QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF VGKKTDKAYW LLEEMLTKEL LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL //